Akao T
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Sugitani, Japan.
Biol Pharm Bull. 1997 Dec;20(12):1245-9. doi: 10.1248/bpb.20.1245.
Glycyrrhetyl mono-glucuronide (GAMG) is an intermediate in the hydrolysis of glycyrrhizin (GL) to glycyrrhetic acid (GA). An enzyme responsible for its hydrolysis, characterized as a GAMG beta-D-glucuronidase of Eubacterium sp. (species) GLH, has been isolated from human intestinal bacteria. The pattern of GAMG beta-D-glucuronidase activity was different from that of GL beta-D-glucuronidase activity by Butyl-Toyopearl 650 S column chromatography. Thus, these enzymes showed differences in the purification ratio and substrate specificity. After this step, GAMG beta-D-glucuronidase was completely separated from GL beta-D-glucuronidase by gel filtration through Toyopearl HW-55 S, indicating that the GAMG beta-D-glucuronidase is a novel type of beta-D-glucuronidase which hydrolyzes one glucuronic acid linkage of GA.
甘草次酸单葡萄糖醛酸苷(GAMG)是甘草酸(GL)水解为甘草次酸(GA)过程中的一种中间体。一种负责其水解的酶,被鉴定为真杆菌属GLH的GAMGβ-D-葡萄糖醛酸酶,已从人体肠道细菌中分离出来。通过丁基-Toyopearl 650 S柱色谱法,GAMGβ-D-葡萄糖醛酸酶活性的模式与GLβ-D-葡萄糖醛酸酶活性的模式不同。因此,这些酶在纯化率和底物特异性方面存在差异。在此步骤之后,通过Toyopearl HW-55 S凝胶过滤将GAMGβ-D-葡萄糖醛酸酶与GLβ-D-葡萄糖醛酸酶完全分离,这表明GAMGβ-D-葡萄糖醛酸酶是一种新型的β-D-葡萄糖醛酸酶,它能水解GA的一个葡萄糖醛酸键。